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8BEF

Cryo-EM structure of the Arabidopsis thaliana I+III2 supercomplex (CI membrane core)

Summary for 8BEF
Entry DOI10.2210/pdb8bef/pdb
EMDB information16000
DescriptorNADH-ubiquinone oxidoreductase chain 3, Outer envelope pore protein 16-3, chloroplastic/mitochondrial, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 13-A, ... (34 entities in total)
Functional Keywordsplant, mitochondria, complex, membrane protein
Biological sourceArabidopsis thaliana (thale cress)
More
Total number of polymer chains22
Total formula weight522385.60
Authors
Klusch, N.,Kuehlbrandt, W. (deposition date: 2022-10-21, release date: 2023-01-11, Last modification date: 2024-10-23)
Primary citationKlusch, N.,Dreimann, M.,Senkler, J.,Rugen, N.,Kuhlbrandt, W.,Braun, H.P.
Cryo-EM structure of the respiratory I + III 2 supercomplex from Arabidopsis thaliana at 2 angstrom resolution.
Nat.Plants, 9:142-156, 2023
Cited by
PubMed Abstract: Protein complexes of the mitochondrial respiratory chain assemble into respiratory supercomplexes. Here we present the high-resolution electron cryo-microscopy structure of the Arabidopsis respiratory supercomplex consisting of complex I and a complex III dimer, with a total of 68 protein subunits and numerous bound cofactors. A complex I-ferredoxin, subunit B14.7 and P9, a newly defined subunit of plant complex I, mediate supercomplex formation. The component complexes stabilize one another, enabling new detailed insights into their structure. We describe (1) an interrupted aqueous passage for proton translocation in the membrane arm of complex I; (2) a new coenzyme A within the carbonic anhydrase module of plant complex I defining a second catalytic centre; and (3) the water structure at the proton exit pathway of complex III with a co-purified ubiquinone in the Q site. We propose that the main role of the plant supercomplex is to stabilize its components in the membrane.
PubMed: 36585502
DOI: 10.1038/s41477-022-01308-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.13 Å)
Structure validation

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数据于2025-06-25公开中

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